| Primary Identifier | IPR036737 | Type | Homologous_superfamily |
| Short Name | OmpA-like_sf |
| description | This entry represents a domain superfamily with a β/α/β/α-β(2) structure found in the C-terminal region of many Gram-negative bacterial outer membrane proteins [], such as porin-like integral membrane proteins (such as ompA) [], small lipid-anchored proteins (such as pal) [], and MotB proton channels []. The N-terminal half is variable although some of the proteins in this group have the OmpA-like transmembrane domain at the N terminus. OmpA from Escherichia coli is required for pathogenesis, and can interact with host receptor molecules []. MotB (and MotA) serves two functions in E. coli, the MotA(4)-MotB(2) complex attaches to the cell wall via MotB to form the stator of the flagellar motor, and the MotA-MotB complex couples the flow of ions across the cell membrane to movement of the rotor [].Other Gram-negative outer membrane proteins with this domain:Outer membrane protein P5 from Haemophilus influenzae.Outer membrane protein P.III/class IV from Neisseria.Outer membrane porin F (gene oprF) from Pseudomonas.Protein TpN50 from Treponema pallidum [].Peptidoglycan-associated lipoprotein (gene pal) from Escherichia coli,Haemophilus influenzae, Legionella pneumophila and Pseudomonas putida.Outer membrane lipoprotein P6 from Haemophilus influenzae.Escherichia coli hypothetical lipoprotein yiaD.Vibrio parahaemolyticus sodium-type flagellar protein motY [, ].The OmpA-like domain is thought to be responsible for non-covalentinteractions with peptidoglycan []. |
